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Database: UniProt
Entry: L5KV02_PTEAL
LinkDB: L5KV02_PTEAL
Original site: L5KV02_PTEAL 
ID   L5KV02_PTEAL            Unreviewed;       392 AA.
AC   L5KV02;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Peroxisomal 3,2-trans-enoyl-CoA isomerase {ECO:0000313|EMBL:ELK15015.1};
GN   ORFNames=PAL_GLEAN10016499 {ECO:0000313|EMBL:ELK15015.1};
OS   Pteropus alecto (Black flying fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC   Pteropodinae; Pteropus.
OX   NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK15015.1, ECO:0000313|Proteomes:UP000010552};
RN   [1] {ECO:0000313|Proteomes:UP000010552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA   Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA   Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA   Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the evolution of
RT   flight and immunity.";
RL   Science 339:456-460(2013).
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DR   EMBL; KB030554; ELK15015.1; -; Genomic_DNA.
DR   RefSeq; XP_006909358.1; XM_006909296.2.
DR   AlphaFoldDB; L5KV02; -.
DR   STRING; 9402.L5KV02; -.
DR   GeneID; 102882135; -.
DR   KEGG; pale:102882135; -.
DR   CTD; 10455; -.
DR   eggNOG; KOG0016; Eukaryota.
DR   eggNOG; KOG0817; Eukaryota.
DR   InParanoid; L5KV02; -.
DR   OrthoDB; 553487at2759; -.
DR   Proteomes; UP000010552; Unassembled WGS sequence.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProt.
DR   GO; GO:0004165; F:delta(3)-delta(2)-enoyl-CoA isomerase activity; IEA:UniProt.
DR   GO; GO:0000062; F:fatty-acyl-CoA binding; IEA:InterPro.
DR   CDD; cd06558; crotonase-like; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 1.10.12.10; Lyase 2-enoyl-coa Hydratase, Chain A, domain 2; 1.
DR   InterPro; IPR022408; Acyl-CoA-binding_prot_CS.
DR   InterPro; IPR000582; Acyl-CoA-binding_protein.
DR   InterPro; IPR035984; Acyl-CoA-binding_sf.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR   InterPro; IPR014748; Enoyl-CoA_hydra_C.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR   PANTHER; PTHR43684; -; 1.
DR   PANTHER; PTHR43684:SF1; ENOYL-COA DELTA ISOMERASE 2; 1.
DR   Pfam; PF00887; ACBP; 1.
DR   Pfam; PF00378; ECH_1; 1.
DR   PRINTS; PR00689; ACOABINDINGP.
DR   SUPFAM; SSF47027; Acyl-CoA binding protein; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 1.
DR   PROSITE; PS00880; ACB_1; 1.
DR   PROSITE; PS51228; ACB_2; 1.
PE   4: Predicted;
KW   Isomerase {ECO:0000313|EMBL:ELK15015.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010552}.
FT   DOMAIN          38..122
FT                   /note="ACB"
FT                   /evidence="ECO:0000259|PROSITE:PS51228"
FT   REGION          119..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   392 AA;  43124 MW;  DD584B25D167ACA3 CRC64;
     MAQRLAKHWC LSAIRSPLQV ISFPALQLHV SGTAMRADQK DFENAVTRVK LLKDPGNEMK
     LKLYALYKQA TEGPCNVPKP GVFNLINKAK WDAWNALGSL PKETARQNYV DLVSSLSSSS
     ASSSQVKPGA DKEQQGSENL VVTSENGITK IMLNRPTKKN AITTQMYQEI ILALKAASKD
     DSTITVLTGN GDYYCSGNDL SNFTDVLSGE IEEKVKSIAI LLRDFVDCFI DFPKPLIAVV
     NGPAVGISVT LLGLFDAVYA SDRATFHTPF SQLGQSPEGC SSYIFPKMMG PAKAKEMLIF
     GKKLTAGEAC AQGLVTEVFP DSTFQTEVWT RLKAYSKLPP NAMRISKQII RNMEKEKLHA
     VNAEEVSVLQ ERWLSDECIN AVMNFLSKRA KL
//
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